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Atomistry » Magnesium » PDB 1cyq-1dak » 1d0z | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 1cyq-1dak » 1d0z » |
Magnesium in PDB 1d0z: Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with P- Nitrophenyl Aminoethyldiphosphate Beryllium Trifluoride.Protein crystallography data
The structure of Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with P- Nitrophenyl Aminoethyldiphosphate Beryllium Trifluoride., PDB code: 1d0z
was solved by
A.M.Gulick,
C.B.Bauer,
J.B.Thoden,
E.Pate,
R.G.Yount,
I.Rayment,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1d0z:
The structure of Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with P- Nitrophenyl Aminoethyldiphosphate Beryllium Trifluoride. also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with P- Nitrophenyl Aminoethyldiphosphate Beryllium Trifluoride.
(pdb code 1d0z). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with P- Nitrophenyl Aminoethyldiphosphate Beryllium Trifluoride., PDB code: 1d0z: Magnesium binding site 1 out of 1 in 1d0zGo back to Magnesium Binding Sites List in 1d0z
Magnesium binding site 1 out
of 1 in the Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with P- Nitrophenyl Aminoethyldiphosphate Beryllium Trifluoride.
Mono view Stereo pair view
Reference:
A.M.Gulick,
C.B.Bauer,
J.B.Thoden,
E.Pate,
R.G.Yount,
I.Rayment.
X-Ray Structures of the Dictyostelium Discoideum Myosin Motor Domain with Six Non-Nucleotide Analogs. J.Biol.Chem. V. 275 398 2000.
Page generated: Tue Aug 13 02:33:44 2024
ISSN: ISSN 0021-9258 PubMed: 10617631 DOI: 10.1074/JBC.275.1.398 |
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